Polyglutamine expansion accelerates the dynamics of ataxin-1 and does not result in aggregate formation (2008)

by H A Krol, P M Krawczyk, K S Bosch, J A Aten, E M Hol, E A Reits
Venue:PLoS One
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© 2009 The Author(s)

by David A. Parfitt, Gregory J. Michael, Esmeralda G. M. Vermeulen, Natalia V, Tom R. Webb, Jean-marc Gallo, Michael E. Cheetham, William S, Gregory L. Blatch , 2009
"... The ataxia protein sacsin is a functional cochaperone that protects against polyglutamine expanded ataxin-1 1 ..."
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The ataxia protein sacsin is a functional cochaperone that protects against polyglutamine expanded ataxin-1 1
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by David A. Parfitt, Gregory J. Michael, Esmeralda G. M. Vermeulen, Natalia V. Prodromou, Tom R. Webb, Jean-marc Gallo, Michael E. Cheetham, William S. Nicoll, Gregory L. Blatch , 2008
"... doi:10.1093/hmg/ddp067 ..."
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doi:10.1093/hmg/ddp067
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aCh

by Biochimica Et Bi , 2015
"... ct w n w enzymeUbcH6modulates the transcriptional repression activity of ATXN1 through ubiquitylation. In the present ites in the AXH domain that are ubiquitylated by UbcH6. Systematic replacement of XH domain revealed that the lysine at 589 (K589) of ATXN1 is essential for its) is an a. The additio ..."
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ct w n w enzymeUbcH6modulates the transcriptional repression activity of ATXN1 through ubiquitylation. In the present ites in the AXH domain that are ubiquitylated by UbcH6. Systematic replacement of XH domain revealed that the lysine at 589 (K589) of ATXN1 is essential for its) is an a. The addition of ubiq-an enzymatic pathway 4,25]. These are the E1 conjugating enzyme)

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by unknown authors
"... al cess appe form s. A Th tim on amyloid fibril formation, and how to avoid common problems that may be encountered, using exam-cated i ’s dise lso ass efined ction, m morphological changes, such as fibril assembly from proto-fibrils to mature fibrils (Fig. 1). The time course of fibril formation ca ..."
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al cess appe form s. A Th tim on amyloid fibril formation, and how to avoid common problems that may be encountered, using exam-cated i ’s dise lso ass efined ction, m morphological changes, such as fibril assembly from proto-fibrils to mature fibrils (Fig. 1). The time course of fibril formation can When studying chaperone-dependent effects on amyloid fibril formation in vitro, two questions may be posed. (1) What is the direct effect of chaperones on fibril formation? (2) What are the mechanisms of the effects of chaperones on amyloid fibril forma-tion? To address the first question, monitoring the effect of chaper-ones on the time course of fibril formation using specific chemical dyes (such as ThT) has often been combined with morphological observations for evaluating the extent of the effect of chaperones (such as by EM or atomic force microscopy, AFM). Measuring the Abbreviations: AFM, atomic force microscopy; DLS, dynamic light scattering; EM, electron microscopy; QCM, quartz crystal microbalance; SEC, size-exclusion
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unknown title

by David A. Parfitt, Gregory J. Michael, Esmeralda G. M. Vermeulen, Natalia V. Prodromou, Tom R. Webb, Jean-marc Gallo, Michael E. Cheetham, William S. Nicoll, Gregory L. Blatch , 2008
"... The ataxia protein sacsin is a functional co-chaperone that protects against polyglutamine-expanded ataxin-1 ..."
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The ataxia protein sacsin is a functional co-chaperone that protects against polyglutamine-expanded ataxin-1
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